Identification |
---|
Name: | 2-octaprenyl-6-methoxyphenol hydroxylase |
---|
Synonyms: | Not Available |
---|
Gene Name: | ubiH |
---|
Enzyme Class: | Not Available |
---|
Biological Properties |
---|
General Function: | Involved in oxidoreductase activity |
---|
Specific Function: | Oxygenase that introduces the hydroxyl group at carbon four of 2-octaprenyl-6-methoxyphenol resulting in the formation of 2-octaprenyl-6-methoxy-1,4-benzoquinone |
---|
Cellular Location: | Not Available |
---|
SMPDB Pathways: | - Secondary Metabolites: Ubiquinol biosynthesis PW000981
- Secondary Metabolites: Ubiquinol biosynthesis 2 PW002036
|
---|
KEGG Pathways: | - Ubiquinone and other terpenoid-quinone biosynthesis ec00130
|
---|
KEGG Reactions: | |
1.02-Polyprenyl-6-methoxyphenol | + | 1.0 | ↔ | 1.02-Polyprenyl-6-methoxy-1,4-benzoquinone | + | 1.0 |
| |
|
---|
SMPDB Reactions: | |
1.0 | + | 1.0NADPH | + | 1.0 | + | 1.0 | + | 1.0 | → | 1.0 | + | 1.0 | + | 1.0 |
| |
|
---|
EcoCyc Reactions: | |
1.0 | + | 1.0 | + | 1.0 | + | 1.0 | → | 1.0 | + | 1.0 | + | 1.0 |
| |
|
---|
Complex Reactions: | |
---|
Metabolites: | |
---|
GO Classification: | Function |
---|
adenyl nucleotide binding | binding | catalytic activity | FAD or FADH2 binding | monooxygenase activity | nucleoside binding | oxidoreductase activity | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NADH or NADPH as one donor, and incorporation of one atom of oxygen | purine nucleoside binding | Process |
---|
cellular metabolic process | coenzyme metabolic process | cofactor metabolic process | metabolic process | oxidation reduction | oxidoreduction coenzyme metabolic process | ubiquinone biosynthetic process | ubiquinone metabolic process |
|
---|
Gene Properties |
---|
Blattner: | b2907 |
---|
Gene Orientation | Counterclockwise |
---|
Centisome Percentage: | 65.75 |
---|
Left Sequence End | 3050362 |
---|
Right Sequence End | 3051540 |
---|
Gene Sequence: | >1179 bp
ATGATCTGGATAATGACGATGGCTCGCCGTATGAACGGTGTTTACGCGGCATTTATGCTG
GTCGCTTTTATGATGGGGGTGGCCGGGGCGCTACAGGCTCCTACATTGAGCTTATTTCTG
AGTCGTGAGGTTGGCGCGCAACCTTTCTGGATCGGCCTCTTTTATACGGTGAATGCTATT
GCTGGGATCGGCGTAAGCCTCTGGTTGGCAAAACGTTCTGACAGTCAGGGCGATCGGCGA
AAACTGATTATATTTTGCTGTTTGATGGCTATCGGCAATGCGCTATTGTTTGCATTTAAT
CGTCATTATCTGACGCTTATCACCTGTGGTGTGCTTCTGGCATCTCTGGCCAATACGGCA
ATGCCACAGTTATTTGCTCTGGCGCGGGAATATGCGGATAACTCGGCGCGAGAAGTGGTG
ATGTTTAGCTCGGTGATGCGTGCGCAGCTTTCTCTGGCATGGGTTATCGGTCCACCGTTG
GCCTTTATGCTGGCGTTGAATTACGGCTTTACGGTGATGTTTTCGATTGCCGCCGGGATA
TTCACACTCAGTCTGGTATTGATTGCATTTATGCTTCCGTCTGTGGCGCGGGTAGAACTG
CCGTCGGAAAATGCTTTATCAATGCAAGGTGGCTGGCAGGATAGTAACGTACGGATGTTA
TTTGTCGCCTCGACGTTAATGTGGACCTGCAACACCATGTACATTATTGATATGCCGTTG
TGGATCAGTAGCGAGTTAGGATTGCCAGACAAACTGGCGGGTTTCCTGATGGGGACGGCA
GCTGGACTGGAAATACCAGCAATGATTCTGGCTGGCTACTATGTCAAACGTTATGGTAAG
CGGCGAATGATGGTCATAGCAGTGGCGGCAGGAGTACTGTTTTACACCGGATTGATTTTC
TTTAATAGCCGTATGGCGTTGATGACGCTGCAACTTTTTAACGCTGTATTTATCGGCATT
GTTGCGGGTATTGGGATGCTATGGTTTCAGGATTTAATGCCTGGAAGAGCGGGGGCAGCT
ACCACCTTATTTACTAACAGTATTTCTACCGGGGTAATTCTGGCTGGCGTTATTCAGGGA
GCAATTGCACAAAGTTGGGGGCACTTTGCTGTCTACTGGGTAATTGCGGTTATTTCTGTT
GTCGCATTATTTTTAACCGCAAAGGTTAAAGACGTTTGA |
---|
Protein Properties |
---|
Pfam Domain Function: | |
---|
Protein Residues: | 392 |
---|
Protein Molecular Weight: | 42288 |
---|
Protein Theoretical pI: | 7 |
---|
Signaling Regions: | |
---|
Transmembrane Regions: | |
---|
Protein Sequence: | >2-octaprenyl-6-methoxyphenol hydroxylase
MSVIIVGGGMAGATLALAISRLSHGALPVHLIEATAPESHAHPGFDGRAIALAAGTCQQL
ARIGVWQSLADCATAITTVHVSDRGHAGFVTLAAEDYQLAALGQVVELHNVGQRLFALLR
KAPGVTLHCPDRVANVARTQSHVEVTLESGETLTGRVLVAADGTHSALATACGVDWQQEP
YEQLAVIANVATSVAHEGRAFERFTQHGPLAMLPMSDGRCSLVWCHPLERREEVLSWSDE
KFCRELQSAFGWRLGKITHAGKRSAYPLALTHAARSITHRTVLVGNAAQTLHPIAGQGFN
LGMRDVMSLAETLTQAQERGEDMGDYGVLCRYQQRRQSDREATIGVTDSLVHLFANRWAP
LVVGRNIGLMTMELFTPARDVLAQRTLGWVAR |
---|
References |
---|
External Links: | |
---|
General Reference: | - Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
- Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
- Nakahigashi, K., Miyamoto, K., Nishimura, K., Inokuchi, H. (1992). "Isolation and characterization of a light-sensitive mutant of Escherichia coli K-12 with a mutation in a gene that is required for the biosynthesis of ubiquinone." J Bacteriol 174:7352-7359. Pubmed: 1339425
|
---|